@inbook{413b789b2ef247d8bf08b67366abb1d8,
title = "Following Molecular Transitions with Single Residue Spatial and Millisecond Time Resolution",
abstract = "{"}Footprinting{"} describes assays in which ligand binding or structure formation protects polymers such as nucleic acids and proteins from either cleavage or modification; footprinting allows the accessibility of individual residues to be mapped in solution. Equilibrium and time-dependent footprinting links site-specific structural information with thermodynamic and kinetic transitions, respectively. The hydroxyl radical (•OH) is a uniquely insightful footprinting probe by virtue of it being among the most reactive chemical oxidants; it reports the solvent accessibility of reactive sites on macromolecules with as fine as a single residue resolution. A novel method of millisecond time-resolved •OH footprinting is presented based on the Fenton reaction, Fe(II) + H2O2 → Fe(III) + •OH + OH-. It is implemented using a standard three-syringe quench-flow mixer. The utility of this method is demonstrated by its application to the studies on RNA folding. Its applicability to a broad range of biological questions involving the function of DNA, RNA, and proteins is discussed.",
author = "Inna Shcherbakova and Somdeb Mitra and Beer, {Robert H.} and Michael Brenowitz",
year = "2008",
month = jan,
day = "1",
doi = "10.1016/S0091-679X(07)84019-2",
language = "English (US)",
isbn = "0123725208",
series = "Methods in Cell Biology",
pages = "589--615",
editor = "John Correi and {Detrich, III}, William",
booktitle = "Biophysical Tools for Biologists, Volume One",
}